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Title 

Chemical modification studies of yeast farnesyl protein transferase

Authors 

Seung Wan SohnGyo JunChul Hak Yang

Publisher 

Springer Verlag (Germany)

Issue Date 

1997

Citation 

Journal of Biochemistry and Molecular Biology, vol. 30, no. 4, pp. 280-284

Keywords 

active sitechemical modificationfarnesyl protein transferase

Abstract 

Phenylglyoxal, diethyl pyrocarbonate (DEPC), and 1-cyclohexyl-3-[2-morpholinoethyl]-carbodiimide metho-p-toluenesulfonate (CMC) are modifying reagents specific for arginine, histidine, and aspartate or glutamate, respectively. They were found to inactivate S. cerevisiae farnesyl protein transferase (FPTase). The peptide substrate protected the enzyme against inactivation by CMC, and the other substrate farnesyl pyrophosphate showed protection against inactivation by phenylglyoxal, while neither of the two substrates protected the enzyme against DEPC inactivation. These results suggest the presence of aspartate/glutamate, arginine and histidine residues at the active site of this enzyme.

ISSN 

1225-8687

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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